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Asma Ressaissi,Nebil Attia,Pedro Luis Fale,Rita Pacheco,Bruno L. Victor,Miguel Machuqueiro,Maria Luı´sa M. Serralheiro 대한약학회 2017 Archives of Pharmacal Research Vol.40 No.11
Bioactive compounds, such as isorhamnetin andpiscidic acid, were obtained from decoctions of cladodes(stem pads from Opuntia ficus-indica). The effect of thesephenolic compounds, in a fiber-free extract, were evaluatedas inhibitors of cholesterol permeation through a Caco-2cell monolayer and as 3-hydroxy-3-methylglutaryl coenzymeA reductase inhibitor. A reduction of 38% incholesterol permeation through the Caco-2 cell monolayerwas obtained, and the phenolic compounds all permeatedbetween 6 and 9%. A mixture of these compounds showedan IC50 of 20.3 lg/mL as an enzyme inhibitor, whereaspiscidic acid alone showed an IC50 of 149.6 lg/mL; thiswas slightly outperformed by the isorhamnetin derivatives. Docking studies confirmed that both piscidic acid andisorhamnetin derivatives, present in the decoction, couldadequately bind to the enzyme active site. These resultsreveal that O. ficus-indica, and cladodes derived therefrom, is a promising plant for use in the development ofnew functional foods and pharmaceutical products.
Serum Albumin Modulates the Bioactivity of Rosmarinic Acid
Elsa Brito,Andre Silva,Pedro Luis Vieira Fale,Rita Pacheco,Antonio Serralheiro,Parvez I. Haris,Lia Ascensao,Maria Luısa Serralheiro 한국식품영양과학회 2018 Journal of medicinal food Vol.21 No.8
Rosmarinic acid (RA) is a phenolic compound with biological activity. The objective of the present study was to investigate whether this compound kept its biological activity in the presence of proteins. For this purpose, bovine serum albumin (BSA) was used as a model protein, and the capacity of the RA to inhibit acetylcholinesterase (AChE) and affect antioxidant activity was evaluated in the absence and presence of BSA. A mixture of phenolic compounds containing RA, obtained from a medicinal plant was added to this study. The AChE inhibitory activity of RA was reduced by ∼57% in the presence of BSA, while the antioxidant activity increased. These results lead to the investigation of the effect of RA on the BSA structure using Fourier transform infrared spectroscopy (FTIR). At 37°C and higher temperatures, RA caused a decrease in the temperature modifications on the protein structure. Furthermore, FTIR and native-gel analysis revealed that protein aggregation/precipitation, induced by temperature, was reduced in the presence of RA. The novelty of the present work resides in the study of the enzyme inhibitory activity and antioxidant capacity of polyphenols, such as RA, in the presence of a protein. The findings highlight the need to consider the presence of proteins when assessing biological activities of polyphenols in vitro and that enzyme inhibitory activity may be decreased, while the antioxidant capacity remains or even increases.